ATP5/YDR298C Summary Help

Standard Name ATP5
Systematic Name YDR298C
Alias OSC1
Feature Type ORF, Verified
Description Subunit 5 of the stator stalk of mitochondrial F1F0 ATP synthase; F1F0 ATP synthase is a large, evolutionarily conserved enzyme complex required for ATP synthesis; homologous to bovine subunit OSCP (oligomycin sensitivity-conferring protein); phosphorylated (1, 2, 3 and see Summary Paragraph)
Name Description ATP synthase
Gene Product Alias oligomycin sensitivity-conferring protein 1
Chromosomal Location
ChrIV:1058814 to 1058176 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gene Ontology Annotations All ATP5 GO evidence and references
  View Computational GO annotations for ATP5
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 5 genes
Classical genetics
Large-scale survey
125 total interaction(s) for 107 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 12
  • Affinity Capture-RNA: 2
  • Affinity Capture-Western: 1
  • Co-purification: 5
  • Reconstituted Complex: 2

Genetic Interactions
  • Negative Genetic: 74
  • Phenotypic Suppression: 2
  • Positive Genetic: 24
  • Synthetic Growth Defect: 1
  • Synthetic Lethality: 1
  • Synthetic Rescue: 1

Expression Summary
Length (a.a.) 212
Molecular Weight (Da) 22,814
Isoelectric Point (pI) 10.37
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrIV:1058814 to 1058176 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..639 1058814..1058176 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000002706

ATP5 encodes the oligomycin sensitivity-conferring protein (OSCP), a subunit of mitochondrial ATP synthase that is homologous to the delta subunit of bacterial ATP synthase (4). The ATP synthase complex utilizes proton motive force to generate ATP from ADP and Pi (4). The structure of this enzyme complex is highly conserved among diverse organisms and consists of two major components, soluble F1 and membrane-bound F0, each of which contains many subunits. F1 and F0 are connected, both functionally and physically, via two additional multi-subunit structures, the central stalk and the stator stalk. OSCP is part of the stator stalk, a stationary structure necessary for the productive transmission of rotary motion from the F0 proton pump to the F1 catalytic core (4 and 5 and references therein).

Although ATP5 is essential for ATP synthase function, it is not essential for life in yeast. Deletion of ATP5, like deletions in many genes necessary for the function or maintenance of mitochondria, leads to a "petite" phenotype that is slow-growing and unable to survive on nonfermentable carbon sources (1).

General ATP synthase structure and function are reviewed in references 4 and 5. For a review that is specific to yeast, see reference 6.

Last updated: 2001-01-16 Contact SGD

References cited on this page View Complete Literature Guide for ATP5
1) Uh M, et al.  (1990) The gene coding for the yeast oligomycin sensitivity-conferring protein. J Biol Chem 265(31):19047-52
2) Soubannier V, et al.  (1999) The second stalk of the yeast ATP synthase complex: identification of subunits showing cross-links with known positions of subunit 4 (subunit b). Biochemistry 38(45):15017-24
3) Reinders J, et al.  (2007) Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase. Mol Cell Proteomics 6(11):1896-906
4) Boyer PD  (1997) The ATP synthase--a splendid molecular machine. Annu Rev Biochem 66:717-49
5) Nakamoto RK, et al.  (1999) Rotational coupling in the F0F1 ATP synthase. Annu Rev Biophys Biomol Struct 28():205-34
6) Devenish RJ, et al.  (2000) Insights into ATP synthase assembly and function through the molecular genetic manipulation of subunits of the yeast mitochondrial enzyme complex. Biochim Biophys Acta 1458(2-3):428-42